Peptidyl-tRNA VII. Substrate specificity of peptidyl-tRNA hydrolase

N. De Groot; Y. Groner; Y. Lapidot

doi:10.1016/0005-2787(69)90006-9

Peptidyl-tRNA VII. Substrate specificity of peptidyl-tRNA hydrolase

N. De Groot^*
, Y. Groner
, Y. Lapidot

^*Corresponding author for this work

Alexander Silberman Institute of Life Sciences

Research output: Contribution to journal › Article › peer-review

25 Scopus citations

Abstract

The enzymatic hydrolysis of peptidyl-tRNA is described. The hydrolysis rates of peptidyl-tRNA with different peptide chain lengths containing free and blocked α-amino groups are compared to the hydrolysis rates of N-acylaminoacyl-tRNA. It is shown that the hydrolysis rate of peptidyl-tRNA containing two peptide bonds is considerably higher than that of N-acylaminoacyl-tRNA. Moreover, the hydrolysis rate of different peptidyl-tRNA's depends on the peptide chain length. Thus, Gly₂-Phe-tRNA is hydrolyzed faster than GlyPhe-tRNA, and Gly₄Phe-tRNA is hydrolyzed faster than Gly₂Phe-tRNA. The apparent K_m and v_max values for Ac-Leu-tRNA are compared to those of Ala₂Leu-tRNA.

Original language	English
Pages (from-to)	286-296
Number of pages	11
Journal	BBA Section Nucleic Acids And Protein Synthesis
Volume	186
Issue number	2
DOIs	https://doi.org/10.1016/0005-2787(69)90006-9
State	Published - 20 Aug 1969

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title = "Peptidyl-tRNA VII. Substrate specificity of peptidyl-tRNA hydrolase",

abstract = "The enzymatic hydrolysis of peptidyl-tRNA is described. The hydrolysis rates of peptidyl-tRNA with different peptide chain lengths containing free and blocked α-amino groups are compared to the hydrolysis rates of N-acylaminoacyl-tRNA. It is shown that the hydrolysis rate of peptidyl-tRNA containing two peptide bonds is considerably higher than that of N-acylaminoacyl-tRNA. Moreover, the hydrolysis rate of different peptidyl-tRNA's depends on the peptide chain length. Thus, Gly2-Phe-tRNA is hydrolyzed faster than GlyPhe-tRNA, and Gly4Phe-tRNA is hydrolyzed faster than Gly2Phe-tRNA. The apparent Km and vmax values for Ac-Leu-tRNA are compared to those of Ala2Leu-tRNA.",

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N2 - The enzymatic hydrolysis of peptidyl-tRNA is described. The hydrolysis rates of peptidyl-tRNA with different peptide chain lengths containing free and blocked α-amino groups are compared to the hydrolysis rates of N-acylaminoacyl-tRNA. It is shown that the hydrolysis rate of peptidyl-tRNA containing two peptide bonds is considerably higher than that of N-acylaminoacyl-tRNA. Moreover, the hydrolysis rate of different peptidyl-tRNA's depends on the peptide chain length. Thus, Gly2-Phe-tRNA is hydrolyzed faster than GlyPhe-tRNA, and Gly4Phe-tRNA is hydrolyzed faster than Gly2Phe-tRNA. The apparent Km and vmax values for Ac-Leu-tRNA are compared to those of Ala2Leu-tRNA.

AB - The enzymatic hydrolysis of peptidyl-tRNA is described. The hydrolysis rates of peptidyl-tRNA with different peptide chain lengths containing free and blocked α-amino groups are compared to the hydrolysis rates of N-acylaminoacyl-tRNA. It is shown that the hydrolysis rate of peptidyl-tRNA containing two peptide bonds is considerably higher than that of N-acylaminoacyl-tRNA. Moreover, the hydrolysis rate of different peptidyl-tRNA's depends on the peptide chain length. Thus, Gly2-Phe-tRNA is hydrolyzed faster than GlyPhe-tRNA, and Gly4Phe-tRNA is hydrolyzed faster than Gly2Phe-tRNA. The apparent Km and vmax values for Ac-Leu-tRNA are compared to those of Ala2Leu-tRNA.

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Peptidyl-tRNA VII. Substrate specificity of peptidyl-tRNA hydrolase

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